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- PDB-4bmf: Solution structure of the cellulose-binding domain of endoglucana... -

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Basic information

Entry
Database: PDB / ID: 4bmf
TitleSolution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello- oligosaccharides
ComponentsENDOGLUCANASE EG-1
KeywordsHYDROLASE / CELLOBIOHYDROLASE
Function / homology
Function and homology information


cellulose binding / cellulase / cellulase activity / cellulose catabolic process / extracellular region
Similarity search - Function
Glycoside hydrolase, family 7 / Glycoside hydrolase family 7, catalytic domain superfamily / Glycosyl hydrolase family 7 / CBM1 (carbohydrate binding type-1) domain signature. / Cellulose-binding domain, fungal / Cellulose-binding domain superfamily / Fungal cellulose binding domain / CBM1 (carbohydrate binding type-1) domain profile. / Fungal-type cellulose-binding domain / Concanavalin A-like lectin/glucanase domain superfamily
Similarity search - Domain/homology
Biological speciesHYPOCREA JECORINA (fungus)
MethodSOLUTION NMR / DISTANCE-GEOMETRY DG REFINED BY SIMULATED ANNEALING SA, AMBER FORCE FIELD IN MOLECULAR DYNAMICS COMPUTATION MD, CONJUGATE GRADIENTS ALGORITHM IN FINAL MINIMIZATION
AuthorsMattinen, M.L. / Linder, M. / Drakenberg, T. / Annila, A.
CitationJournal: Eur.J.Biochem. / Year: 1998
Title: Solution Structure of the Cellulose-Binding Domain of Endoglucanase I from Trichoderma Reesei and its Interaction with Cello-Oligosaccharides.
Authors: Mattinen, M.L. / Linder, M. / Drakenberg, T. / Annila, A.
History
DepositionMay 8, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 22, 2013Provider: repository / Type: Initial release
Revision 1.1May 29, 2013Group: Atomic model
Revision 1.2Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ENDOGLUCANASE EG-1


Theoretical massNumber of molelcules
Total (without water)4,0951
Polymers4,0951
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)19 / 100LEAST RESTRAINT VIOLATIN
Representative

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Components

#1: Protein/peptide ENDOGLUCANASE EG-1 / ENDOGLUCANASE I / CELLULASE / ENDO-1 / 4-BETA-GLUCANASE


Mass: 4095.447 Da / Num. of mol.: 1 / Fragment: CELLULOSE-BINDING DOMAIN, RESIDUES 422-459 / Source method: obtained synthetically / Source: (synth.) HYPOCREA JECORINA (fungus) / References: UniProt: P07981, cellulase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131COSY
NMR detailsText: NONE

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Sample preparation

DetailsContents: 10% D2O AND 90 H2O
Sample conditionspH: 3.9 / Temperature: 293.0 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Insight IIIIACCELERYS, INCrefinement
DG IIIIstructure solution
Insight II95structure solution
Discoverstructure solution
BIOSYM TECHNOLOGIESTECHNOLOGIESstructure solution
RefinementMethod: DISTANCE-GEOMETRY DG REFINED BY SIMULATED ANNEALING SA, AMBER FORCE FIELD IN MOLECULAR DYNAMICS COMPUTATION MD, CONJUGATE GRADIENTS ALGORITHM IN FINAL MINIMIZATION
Software ordinal: 1
Details: AMBER FORCE FIELD WAS USED IN THE MOLECULAR DYNAMICS COMPUTATION MD AND THE GONJUGATE GRADIENTS ALGORITHIM IN THE FINAL MINIMIZATION
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATIN / Conformers calculated total number: 100 / Conformers submitted total number: 19

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